Origins and implications of the D stagger in collagen
Although the distribution of hydrophobic residues in the α1 chain collagen sequence has a D ⋍ 670 Å periodicity, it is dipoles formed by 100 residues occurring in pairs of unlike charge which are responsible for the 1D stagger between molecules. Sheet models based on the Hodge-Petruska model for the...
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Veröffentlicht in: | Biochemical and biophysical research communications 1974-09, Vol.60 (2), p.858-864 |
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Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | Although the distribution of hydrophobic residues in the α1 chain collagen sequence has a D ⋍ 670 Å periodicity, it is dipoles formed by 100 residues occurring in pairs of unlike charge which are responsible for the 1D stagger between molecules. Sheet models based on the Hodge-Petruska model for the axially projected collagen structure require interactions specifying 1D and 4D staggers. We found no evidence for interactions specifying a strong 4D stagger and, therefore, favour the Smith microfibril model which is specified by 1D stagger interactions alone. Two hydroxylysine residues, 234 residues apart, may form a covalent cross-link stabilising the 1D stagger. Gene duplication does not appear to be responsible for the periodicity in the sequence. |
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ISSN: | 0006-291X 1090-2104 |
DOI: | 10.1016/0006-291X(74)90320-9 |